SARS-CoV-2 Spike Glycoprotein Receptor Binding Domain K417N, E484K, N501Y variant (rabbit IgG1 Fc-tagged)

SARS-CoV-2 Spike RBD|SARS-CoV-2 Spike Receptor Binding Domain|Severe Acute Respiratory Syndrome Coronavirus 2 Spike Glycoprotein Receptor Binding Domain|South African Variant|Spike S1 RBD|WHO Label: Beta

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is an enveloped positive-stranded RNA virus, a member of the Betacoronavirus genus, and the causative agent of COVID-19.{53462,53459,53461,55257,55258} The SARS-CoV-2 spike glycoprotein, also known as the surface glycoprotein, is located on the outer envelope of the virion.{53462} It is composed of an S1 and S2 subunit divided by a furin S-cleavage site not found in other SARS-CoVs.{46767,49561} The S1 subunit contains the receptor-binding domain (RBD), which binds to the carboxypeptidase angiotensin-converting enzyme 2 (ACE2), and the S1 and S2 subunits are cleaved by the protease TMPRSS2 to facilitate viral fusion with the host cell membrane.{49542,49536,49558} In this way, ACE2 acts as the functional receptor for SARS-CoV-2. The SARS-CoV-2 variant of concern (VOC) B.1.351, originally identified in South Africa, contains three substitutions located within the spike glycoprotein RBD.{60562,61502} The lysine-to-asparagine substitution at position 417 (K417N) reduces SARS-CoV-2 affinity for human ACE2, whereas the glutamate-to-lysine substitution at position 484 (E484K) and the asparagine-to-tyrosine substitution at position 501 (N501Y) increase SARS-CoV-2 affinity for human ACE2.{60562} Collectively, the K417N, E484K, and N501Y substitutions are associated with enhanced viral infectivity and resistance to antibody-mediated neutralization.{61502} Cayman's SARS-CoV-2 Spike Glycoprotein Receptor Binding Domain K417N, E484K, N501Y variant (rabbit IgG1 Fc-tagged) can be used for ELISA, surface plasmon resonance (SPR), and Western blot applications.

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PBS, pH 7.4, with 5% mannitol, 5% trehalose, 0.01% polysorbate 20, and 10% glycerol

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≥90% (estimated by SDS-PAGE)